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Protein

Endo-alpha-N-acetylgalactosaminidase

Gene

spr0328

Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Is involved in the breakdown of mucin-type O-linked glycans. Specifically removes the T-antigen disaccharide (Gal-beta-1,3-GalNAc-alpha) from extracellular host glycoproteins. Is representative of a broadly important class of virulence factors.3 Publications

Catalytic activityi

3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H2O = 3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein].1 Publication

Kineticsi

  1. KM=34 µM for Gal-beta-1,3-GalNAc-alpha-2,4-dinitrophenyl1 Publication

    pH dependencei

    Optimum pH is 7.6.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi577 – 5771Calcium 11 Publication
    Metal bindingi579 – 5791Calcium 11 Publication
    Metal bindingi581 – 5811Calcium 11 Publication
    Metal bindingi583 – 5831Calcium 1; via carbonyl oxygen1 Publication
    Metal bindingi588 – 5881Calcium 11 Publication
    Binding sitei658 – 6581SubstrateCurated
    Active sitei764 – 7641Nucleophile1 Publication
    Active sitei796 – 7961Proton donor/Proton acceptor1 Publication
    Metal bindingi1233 – 12331Calcium 2; via carbonyl oxygen1 Publication
    Metal bindingi1235 – 12351Calcium 21 Publication
    Metal bindingi1281 – 12811Calcium 2; via carbonyl oxygen1 Publication
    Metal bindingi1284 – 12841Calcium 2; via carbonyl oxygen1 Publication
    Metal bindingi1411 – 14111Calcium 21 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Virulence

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciSPNE171101:GJC8-335-MONOMER.
    BRENDAi3.2.1.97. 11933.

    Protein family/group databases

    CAZyiCBM32. Carbohydrate-Binding Module Family 32.
    GH101. Glycoside Hydrolase Family 101.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-alpha-N-acetylgalactosaminidase (EC:3.2.1.97)
    Alternative name(s):
    SpGH101
    Gene namesi
    Ordered Locus Names:spr0328
    OrganismiStreptococcus pneumoniae (strain ATCC BAA-255 / R6)
    Taxonomic identifieri171101 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    Proteomesi
    • UP000000586 Componenti: Chromosome

    Subcellular locationi

    • Secretedcell wall PROSITE-ProRule annotation; Peptidoglycan-anchor PROSITE-ProRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell wall, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi658 – 6581D → A: Large decrease in substrate affinity. 1 Publication
    Mutagenesisi764 – 7641D → A: Loss of activity. 1 Publication
    Mutagenesisi796 – 7961E → A or Q: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3939Sequence analysisAdd
    BLAST
    Chaini40 – 17381699Endo-alpha-N-acetylgalactosaminidasePRO_0000408870Add
    BLAST
    Propeptidei1739 – 176729Removed by sortasePROSITE-ProRule annotationPRO_0000408871Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1738 – 17381Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation

    Keywords - PTMi

    Peptidoglycan-anchor

    Interactioni

    Protein-protein interaction databases

    STRINGi171101.spr0328.

    Structurei

    Secondary structure

    1
    1767
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi124 – 1274Combined sources
    Helixi131 – 1333Combined sources
    Beta strandi136 – 1427Combined sources
    Beta strandi145 – 1517Combined sources
    Beta strandi158 – 1614Combined sources
    Beta strandi163 – 1675Combined sources
    Beta strandi178 – 1869Combined sources
    Beta strandi195 – 2039Combined sources
    Beta strandi206 – 2138Combined sources
    Beta strandi216 – 2227Combined sources
    Beta strandi243 – 2508Combined sources
    Beta strandi255 – 2606Combined sources
    Helixi273 – 2797Combined sources
    Beta strandi284 – 2896Combined sources
    Beta strandi298 – 3025Combined sources
    Beta strandi331 – 3355Combined sources
    Beta strandi337 – 34812Combined sources
    Beta strandi350 – 3556Combined sources
    Beta strandi358 – 3625Combined sources
    Beta strandi370 – 3723Combined sources
    Beta strandi375 – 3773Combined sources
    Beta strandi380 – 3878Combined sources
    Beta strandi390 – 39910Combined sources
    Helixi400 – 4023Combined sources
    Beta strandi404 – 41512Combined sources
    Beta strandi418 – 43013Combined sources
    Helixi441 – 4433Combined sources
    Beta strandi447 – 4493Combined sources
    Beta strandi455 – 4595Combined sources
    Beta strandi466 – 4705Combined sources
    Beta strandi481 – 4855Combined sources
    Beta strandi494 – 50310Combined sources
    Beta strandi508 – 5136Combined sources
    Beta strandi519 – 5213Combined sources
    Helixi522 – 5243Combined sources
    Beta strandi529 – 5379Combined sources
    Beta strandi539 – 5468Combined sources
    Helixi562 – 5643Combined sources
    Beta strandi569 – 5768Combined sources
    Beta strandi578 – 5825Combined sources
    Helixi586 – 5938Combined sources
    Turni594 – 5963Combined sources
    Helixi603 – 6086Combined sources
    Beta strandi609 – 6168Combined sources
    Helixi626 – 64015Combined sources
    Beta strandi644 – 6507Combined sources
    Helixi669 – 6713Combined sources
    Helixi673 – 68513Combined sources
    Turni686 – 6883Combined sources
    Beta strandi689 – 70012Combined sources
    Beta strandi704 – 7063Combined sources
    Turni709 – 7113Combined sources
    Beta strandi722 – 73312Combined sources
    Helixi735 – 7406Combined sources
    Helixi743 – 75412Combined sources
    Beta strandi760 – 7656Combined sources
    Helixi776 – 78712Combined sources
    Turni788 – 7903Combined sources
    Beta strandi792 – 7965Combined sources
    Beta strandi798 – 8003Combined sources
    Turni802 – 8043Combined sources
    Beta strandi806 – 8083Combined sources
    Helixi809 – 8124Combined sources
    Beta strandi814 – 8174Combined sources
    Beta strandi821 – 8233Combined sources
    Helixi827 – 8337Combined sources
    Turni834 – 8363Combined sources
    Helixi845 – 8473Combined sources
    Helixi849 – 8513Combined sources
    Beta strandi864 – 8663Combined sources
    Helixi867 – 8693Combined sources
    Helixi874 – 89017Combined sources
    Beta strandi893 – 9008Combined sources
    Beta strandi904 – 9085Combined sources
    Beta strandi911 – 9155Combined sources
    Beta strandi918 – 9247Combined sources
    Beta strandi930 – 9367Combined sources
    Helixi943 – 9464Combined sources
    Beta strandi948 – 9525Combined sources
    Beta strandi955 – 9595Combined sources
    Beta strandi962 – 9676Combined sources
    Helixi978 – 9803Combined sources
    Beta strandi982 – 9898Combined sources
    Beta strandi991 – 9966Combined sources
    Helixi999 – 10024Combined sources
    Beta strandi1007 – 10126Combined sources
    Beta strandi1015 – 10217Combined sources
    Beta strandi1026 – 10327Combined sources
    Beta strandi1039 – 10446Combined sources
    Turni1053 – 10586Combined sources
    Beta strandi1072 – 10765Combined sources
    Helixi1078 – 10803Combined sources
    Beta strandi1081 – 10855Combined sources
    Beta strandi1091 – 10955Combined sources
    Beta strandi1097 – 11004Combined sources
    Beta strandi1102 – 11076Combined sources
    Beta strandi1116 – 112510Combined sources
    Beta strandi1127 – 11293Combined sources
    Beta strandi1131 – 11366Combined sources
    Beta strandi1141 – 11488Combined sources
    Helixi1164 – 11663Combined sources
    Beta strandi1176 – 11838Combined sources
    Beta strandi1192 – 11976Combined sources
    Beta strandi1199 – 12024Combined sources
    Beta strandi1204 – 121310Combined sources
    Beta strandi1219 – 12213Combined sources
    Beta strandi1223 – 12253Combined sources
    Beta strandi1230 – 12323Combined sources
    Turni1240 – 12434Combined sources
    Beta strandi1244 – 12463Combined sources
    Beta strandi1251 – 12544Combined sources
    Beta strandi1256 – 12616Combined sources
    Turni1264 – 12674Combined sources
    Helixi1271 – 12733Combined sources
    Beta strandi1284 – 12907Combined sources
    Beta strandi1296 – 13016Combined sources
    Turni1303 – 13053Combined sources
    Beta strandi1313 – 132412Combined sources
    Beta strandi1327 – 133610Combined sources
    Beta strandi1339 – 13413Combined sources
    Helixi1346 – 13483Combined sources
    Beta strandi1349 – 13535Combined sources
    Beta strandi1365 – 13728Combined sources
    Beta strandi1379 – 13857Combined sources
    Helixi1397 – 14037Combined sources
    Turni1404 – 14063Combined sources
    Beta strandi1407 – 141812Combined sources
    Helixi1422 – 143716Combined sources
    Helixi1444 – 14507Combined sources
    Helixi1452 – 14587Combined sources
    Helixi1466 – 147510Combined sources
    Helixi1477 – 14804Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ECQX-ray2.90A/B40-1567[»]
    ProteinModelPortaliQ8DR60.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8DR60.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni602 – 893292CatalyticAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1735 – 17395LPXTG sorting signalPROSITE-ProRule annotation

    Domaini

    Is a multimodular protein that comprises seven distinct domains. The catalytic glycoside hydrolase domain resides in domain 3 (residues 602-893). Possesses four potential carbohydrate-binding modules (CBMs).1 Publication

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105ESP. Bacteria.
    ENOG410XRFZ. LUCA.
    HOGENOMiHOG000285069.
    KOiK17624.
    OMAiWHTSWNG.

    Family and domain databases

    CDDicd14244. GH_101_like. 1 hit.
    Gene3Di2.60.120.260. 1 hit.
    InterProiIPR025706. Endoa_GalNAc.
    IPR000421. FA58C.
    IPR008979. Galactose-bd-like.
    IPR005877. YSIRK_signal_dom.
    [Graphical view]
    PfamiPF00754. F5_F8_type_C. 1 hit.
    PF12905. Glyco_hydro_101. 1 hit.
    PF04650. YSIRK_signal. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    TIGRFAMsiTIGR01168. YSIRK_signal. 1 hit.
    PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8DR60-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNKGLFEKRC KYSIRKFSLG VASVMIGATF FGTSPVLADS VQSGSTANLP
    60 70 80 90 100
    ADLATALATA KENDGHDFEA PKVGEDQGSP EVTDGPKTEE ELLALEKEKP
    110 120 130 140 150
    AEEKPKEDKP AAAKPETPKT VTPEWQTVEK KEQQGTVTIR EEKGVRYNQL
    160 170 180 190 200
    SSTAQNDNAG KPALFEKKGL TVDANGNATV DLTFKDDSEK GKSRFGVFLK
    210 220 230 240 250
    FKDTKNNVFV GYDKDGWFWE YKSPTTSTWY RGSRVAAPET GSTNRLSITL
    260 270 280 290 300
    KSDGQLNASN NDVNLFDTVT LPAAVNDHLK NEKKILLKAG SYDDERTVVS
    310 320 330 340 350
    VKTDNQEGVK TEDTPAEKET GPEVDDSKVT YDTIQSKVLK AVIDQAFPRV
    360 370 380 390 400
    KEYSLNGHTL PGQVQQFNQV FINNHRITPE VTYKKINETT AEYLMKLRDD
    410 420 430 440 450
    AHLINAEMTV RLQVVDNQLH FDVTKIVNHN QVTPGQKIDD ERKLLSSISF
    460 470 480 490 500
    LGNALVSVSS DQTGAKFDGA TMSNNTHVSG DDHIDVTNPM KDLAKGYMYG
    510 520 530 540 550
    FVSTDKLAAG VWSNSQNSYG GGSNDWTRLT AYKETVGNAN YVGIHSSEWQ
    560 570 580 590 600
    WEKAYKGIVF PEYTKELPSA KVVITEDANA DKKVDWQDGA IAYRSIMNNP
    610 620 630 640 650
    QGWKKVKDIT AYRIAMNFGS QAQNPFLMTL DGIKKINLHT DGLGQGVLLK
    660 670 680 690 700
    GYGSEGHDSG HLNYADIGKR IGGVEDFKTL IEKAKKYGAH LGIHVNASET
    710 720 730 740 750
    YPESKYFNEK ILRKNPDGSY SYGWNWLDQG INIDAAYDLA HGRLARWEDL
    760 770 780 790 800
    KKKLGDGLDF IYVDVWGNGQ SGDNGAWATH VLAKEINKQG WRFAIEWGHG
    810 820 830 840 850
    GEYDSTFHHW AADLTYGGYT NKGINSAITR FIRNHQKDAW VGDYRSYGGA
    860 870 880 890 900
    ANYPLLGGYS MKDFEGWQGR SDYNGYVTNL FAHDVMTKYF QHFTVSKWEN
    910 920 930 940 950
    GTPVTMTDNG STYKWTPEMR VELVDADNNK VVVTRKSNDV NSPQYRERTV
    960 970 980 990 1000
    TLNGRVIQDG SAYLTPWNWD ANGKKLSTDK EKMYYFNTQA GATTWTLPSD
    1010 1020 1030 1040 1050
    WAKSKVYLYK LTDQGKTEEQ ELTVKDGKIT LDLLANQPYV LYRSKQTNPE
    1060 1070 1080 1090 1100
    MSWSEGMHIY DQGFNSGTLK HWTISGDASK AEIVKSQGAN DMLRIQGNKE
    1110 1120 1130 1140 1150
    KVSLTQKLTG LKPNTKYAVY VGVDNRSNAK ASITVNTGEK EVTTYTNKSL
    1160 1170 1180 1190 1200
    ALNYVKAYAH NTRRNNATVD DTSYFQNMYA FFTTGSDVSN VTLTLSREAG
    1210 1220 1230 1240 1250
    DEATYFDEIR TFENNSSMYG DKHDTGKGTF KQDFENVAQG IFPFVVGGVE
    1260 1270 1280 1290 1300
    GVEDNRTHLS EKHDPYTQRG WNGKKVDDVI EGNWSLKTNG LVSRRNLVYQ
    1310 1320 1330 1340 1350
    TIPQNFRFEA GKTYRVTFEY EAGSDNTYAF VVGKGEFQSG RRGTQASNLE
    1360 1370 1380 1390 1400
    MHELPNTWTD SKKAKKATFL VTGAETGDTW VGIYSTGNAS NTRGDSGGNA
    1410 1420 1430 1440 1450
    NFRGYNDFMM DNLQIEEITL TGKMLTENAL KNYLPTVAMT NYTKESMDAL
    1460 1470 1480 1490 1500
    KEAVFNLSQA DDDISVEEAR AEIAKIEALK NALVQKKTAL VADDFASLTA
    1510 1520 1530 1540 1550
    PAQAQEGLAN AFDGNLSSLW HTSWGGGDVG KPATMVLKEA TEITGLRYVP
    1560 1570 1580 1590 1600
    RGSGSNGNLR DVKLVVTDES GKEHTFTATD WPDNNKPKDI DFGKTIKAKK
    1610 1620 1630 1640 1650
    IVLTGTKTYG DGGDKYQSAA ELIFTRPQVA ETPLDLSGYE AALAKAQKLT
    1660 1670 1680 1690 1700
    DKDNQEEVAS VQASMKYATD NHLLTERMVE YFADYLNQLK DSATKPDAPT
    1710 1720 1730 1740 1750
    VEKPEFKLSS VASDQGKTPD YKQEIARPET PEQILPATGE SQFDTALFLA
    1760
    SVSLALSALF VVKTKKD
    Length:1,767
    Mass (Da):196,144
    Last modified:March 1, 2003 - v1
    Checksum:i34231975797B7587
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE007317 Genomic DNA. Translation: AAK99132.1.
    PIRiH97912.
    RefSeqiNP_357922.1. NC_003098.1.
    WP_001032523.1. NC_003098.1.

    Genome annotation databases

    EnsemblBacteriaiAAK99132; AAK99132; spr0328.
    GeneIDi934804.
    KEGGispr:spr0328.
    PATRICi19700491. VBIStrPne107296_0367.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE007317 Genomic DNA. Translation: AAK99132.1.
    PIRiH97912.
    RefSeqiNP_357922.1. NC_003098.1.
    WP_001032523.1. NC_003098.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ECQX-ray2.90A/B40-1567[»]
    ProteinModelPortaliQ8DR60.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi171101.spr0328.

    Protein family/group databases

    CAZyiCBM32. Carbohydrate-Binding Module Family 32.
    GH101. Glycoside Hydrolase Family 101.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAK99132; AAK99132; spr0328.
    GeneIDi934804.
    KEGGispr:spr0328.
    PATRICi19700491. VBIStrPne107296_0367.

    Phylogenomic databases

    eggNOGiENOG4105ESP. Bacteria.
    ENOG410XRFZ. LUCA.
    HOGENOMiHOG000285069.
    KOiK17624.
    OMAiWHTSWNG.

    Enzyme and pathway databases

    BioCyciSPNE171101:GJC8-335-MONOMER.
    BRENDAi3.2.1.97. 11933.

    Miscellaneous databases

    EvolutionaryTraceiQ8DR60.

    Family and domain databases

    CDDicd14244. GH_101_like. 1 hit.
    Gene3Di2.60.120.260. 1 hit.
    InterProiIPR025706. Endoa_GalNAc.
    IPR000421. FA58C.
    IPR008979. Galactose-bd-like.
    IPR005877. YSIRK_signal_dom.
    [Graphical view]
    PfamiPF00754. F5_F8_type_C. 1 hit.
    PF12905. Glyco_hydro_101. 1 hit.
    PF04650. YSIRK_signal. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    TIGRFAMsiTIGR01168. YSIRK_signal. 1 hit.
    PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGH101_STRR6
    AccessioniPrimary (citable) accession number: Q8DR60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 31, 2011
    Last sequence update: March 1, 2003
    Last modified: September 7, 2016
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The hydrolysis reaction catalyzed by SpGH101 proceeds with retention of the anomeric configuration.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.